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Literature summary extracted from

  • Murfitt, L.M.; Kolosova, N.; Mann, C.J.; Dudareva, N.
    Purification and characterization of S-adenosyl-L-methionine:benzoic acid carboxyl methyltransferase, the enzyme responsible for biosynthesis of the volatile ester methyl benzoate in flowers of Antirrhinum majus (2000), Arch. Biochem. Biophys., 382, 145-151.
    View publication on PubMed

Inhibitors

EC Number Inhibitors Comment Organism Structure
2.1.1.273 Ca2+ 5 mM, slight inhibitory effect, less than 10% inhibition Antirrhinum majus
2.1.1.273 Cu2+ 5 mM, strong inhibitory effect, 75–100% inhibition Antirrhinum majus
2.1.1.273 Fe2+ 5 mM, strong inhibitory effect, 75–100% inhibition Antirrhinum majus
2.1.1.273 Mn2+ 5 mM, slight inhibitory effect, less than 10% inhibition Antirrhinum majus
2.1.1.273 Na+ 5 mM, slight inhibitory effect, less than 10% inhibition Antirrhinum majus
2.1.1.273 S-adenosyl-L-homocysteine competitive inhibition with respect to S-adenosyl-L-methionine and noncompetitive inhibition with respect to benzoate Antirrhinum majus
2.1.1.273 Zn2+ 5 mM, slight inhibitory effect, less than 10% inhibition Antirrhinum majus

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
2.1.1.273 0.028
-
 S-adenosyl-L-methionine apparent Km-value of plant-purified protein, pH 7.5, 20°C Antirrhinum majus
2.1.1.273 0.087
-
 S-adenosyl-L-methionine apparent Km-value of recombinant protein, pH 7.5, 20°C Antirrhinum majus
2.1.1.273 1.1
-
 benzoate apparent Km-value of plant-purified protein, pH 7.5, 20°C Antirrhinum majus
2.1.1.273 1.6
-
 benzoate apparent Km-value of recombinant protein, pH 7.5, 20°C Antirrhinum majus

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
2.1.1.273 K+ 5 mM, stimulates BAMT activity by a factor of 2 Antirrhinum majus
2.1.1.273 Mg2+ BAMT activity not affected by the presence of 5 mM Antirrhinum majus
2.1.1.273 NH4+ 5 mM, stimulates BAMT activity by a factor of 2 Antirrhinum majus

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
2.1.1.273 41000
-
 calculated molecular mass of the protein encoded by BAMT cDNA Antirrhinum majus
2.1.1.273 49000
-
 denatured protein, SDS–PAGE Antirrhinum majus
2.1.1.273 100000
-
 native protein, gel filtration chromatography on Superdex 200-HR Antirrhinum majus

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
2.1.1.273 S-adenosyl-L-methionine + benzoate Antirrhinum majus
-
 S-adenosyl-L-homocysteine + methyl benzoate
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
2.1.1.273 Antirrhinum majus
-
 snapdragon
-

Purification (Commentary)

EC Number Purification (Comment) Organism
2.1.1.273 enzyme purified from upper and lower petal lobes of 5- to 10-day-old snapdragon flowers using DE53 anion exchange chromatography, hydrophobic interaction chromatography using Phenyl-Sepharose 6FF, and Mono-Q chromatography Antirrhinum majus

Reaction

EC Number Reaction Comment Organism Reaction ID
2.1.1.273 S-adenosyl-L-methionine + benzoate = S-adenosyl-L-homocysteine + methyl benzoate ordered bi–bi mechanism, derived from kinetic analysis, S-adenosyl-L-methionine appears to be the first substrate to bind to the enzyme and methyl benzoate would be the first to be released and S-adenosyl-L-homocysteine the last Antirrhinum majus
a

Source Tissue

EC Number Source Tissue Comment Organism Textmining
2.1.1.273 petal enzyme is expressed in the upper and lower lobes of petals of snapdragon flowers Antirrhinum majus
-

Specific Activity [micromol/min/mg]

EC Number Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
2.1.1.273 0.01962
-
 purified BAMT protein, pH 7.5, 20°C Antirrhinum majus

Storage Stability

EC Number Storage Stability Organism
2.1.1.273 the purified proteins, both from petal tissue and from Escherichia coli, are highly stable for several months when stored at -80°C. When stored in a buffer containing 50 mM Bis–Tris–HCl, pH 6.9, 10% glycerol, and 10 mM beta-mercaptoethanol at 4°C, BAMT protein is stable for 1 week Antirrhinum majus

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.1.1.273 additional information no activity toward other naturally occurring substrates like salicylic acid, trans-cinnamic acid, and their derivatives 3-hydroxybenzoic acid, 4-hydroxybenzoic acid, benzyl alcohol, and 2-coumaric, 3-coumaric, and 4-coumaric acid Antirrhinum majus ?
-
 ?
2.1.1.273 S-adenosyl-L-methionine + benzoate
-
 Antirrhinum majus S-adenosyl-L-homocysteine + methyl benzoate
-
 ?

Subunits

EC Number Subunits Comment Organism
2.1.1.273 homodimer 2 * 49000 Antirrhinum majus

Synonyms

EC Number Synonyms Comment Organism
2.1.1.273 BAMT
-
 Antirrhinum majus

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
2.1.1.273 20
-
-
 Antirrhinum majus

Temperature Stability [°C]

EC Number Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
2.1.1.273 20 65 BAMT is 100% stable for 30 min at 20°C and 60% stable for 30 min at 30°C, it is 20% stable for 30 min at 42°C but after 30 min incubation at 65°C, it completely loses activity Antirrhinum majus

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
2.1.1.273 7.5
-
-
 Antirrhinum majus

pH Range

EC Number pH Minimum pH Maximum Comment Organism
2.1.1.273 additional information
-
 the enzyme is active in both Tris- and phosphate–citrate-based buffers Antirrhinum majus
2.1.1.273 5.5 9.5 with 65% of maximum activity at both pH 6.5 and 8.5 and at pH 5.5 and 9.5, the enzyme activity falls to about 50% of the optimal value Antirrhinum majus

Ki Value [mM]

EC Number Ki Value [mM] Ki Value maximum [mM] Inhibitor Comment Organism Structure
2.1.1.273 0.007
-
 S-adenosyl-L-homocysteine for S-adenosyl-L-methionine, pH 7.5, 20°C Antirrhinum majus
2.1.1.273 0.014
-
 S-adenosyl-L-homocysteine for benzoate, pH 7.5, 20°C Antirrhinum majus